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EXPRESSION OF HUMAN INTERLEUKIN-33 FUSED WITH SUMO IN ESCHERICHIA COLI
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Abstract
Background: Recent studies showed that interleukin (IL)-33 and its receptor play an important role in inflammation, infection, and autoimmune diseases. Nevetheless, direct extractions of IL-33 from human tissues often resulted in limited amount of this cytokine, which may hinder the drug discovery process. Objectives: This study aims to express recombinant human IL-33 fused with SUMO in Escherichia coli. Methods: codons from human il33 gene was optimized for the expression in E. coli using OptimumGeneTM Optimization Analysis (GeneScript). The recombinant plasmid pET-SUMO-il33 was transformed into chemically compentent E. coli BL21 (DE3) by heat-shock method. Results: The recombinant plasmid was designed with a 8×His and a SUMO tag at the N-terminal of the codon-optimized il33 gene. The transformed E. coli BL21(DE3) could express soluble recombinant IL-33 in LB medium at 37°C. Conclusion: In this study, we have successfully transformed E. coli BL21(DE3) with the recombinant plasmid pET-SUMO-il33. The bacteria could express soluble SUMO-IL-33 with high yield.
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Keywords
recombinant human interleukin-33, codon optimization, pET-SUMO, E. coli
References
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